ArticleACS chemical biology2015
Synergistic binding of the leader and core peptides by the lantibiotic synthetase HalM2.
Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Structural insights into the substrate binding mechanism of the class I dehydratase MadB.Communications biology · 2025Article
- Anticancer Ribosomally Synthesized and Post-Translationally Modified Peptides from Plants: Structures, Therapeutic Potential, and Future Directions.Current issues in molecular biology · 2024Review
- The structure of MadC fromFrontiers in microbiology · 2022Article
- Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB.Nature chemical biology · 2021Article
- Substrate Recognition by the Class II Lanthipeptide Synthetase HalM2.ACS chemical biology · 2020Article
- A Structural View on the Maturation of Lanthipeptides.Frontiers in microbiology · 2020Review
- Roads to Rome: Role of Multiple Cassettes in Cyanobactin RiPP Biosynthesis.Journal of the American Chemical Society · 2018Article
- Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.Chemical reviews · 2017Review
- One-pot synthesis of class II lanthipeptide bovicin HJ50 via an engineered lanthipeptide synthetase.Scientific reports · 2016Article
- Structural Characterization and Bioactivity Analysis of the Two-Component Lantibiotic Flv System from a Ruminant Bacterium.Cell chemical biology · 2016Article
- New Insights into the Biosynthetic Logic of Ribosomally Synthesized and Post-translationally Modified Peptide Natural Products.Cell chemical biology · 2016Review
- Article
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5 authors.
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Abstract
Lanthipeptides are a class of ribosomally produced and post-translationally modified peptides (RiPPs) that possess a variety of biological activities but typically act as antimicrobial agents (lantibiotics). Haloduracin is a lantibiotic that is composed of two post-translationally modified peptides, Halα and Halβ, which are biosynthesized from the precursor peptides HalA1 and HalA2 by their cognate lanthipeptide synthetases, HalM1 and HalM2, respectively. Coexpression studies of HalM1 and HalM2 with chimeric peptides consisting of the leader peptide of HalA1 and the core peptide of HalA2 (or vice versa) showed that the synthetases require both the cognate leader and core peptides for efficient processing. Investigation of the affinity in vitro showed that binding of the N-terminal leader peptide by HalM2 increases its affinity for the C-terminal core peptide. Thus, the two segments of the precursor peptide HalA2 synergistically bind to HalM2.
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